A potentially useful cyanobacterial sulfated exopolysaccharide and its biosynthesis and regulation genes, which contribute to the laboratorial bloom formation, are elucidated for the first time among prokaryotes.

The structure of the photosystem I (PSI) complex from Synechocystis is determined, and reaction center subunits engineered to resemble a viral PSI are found to promote promiscuous electron acceptor properties.

In vivo evidence is provided indicating that Flv2/Flv4, together with Flv1/Flv3, mediate O₂ photoreduction downstream of PSI in a highly coordinated manner.

The necessity of studying extremophile organisms is exemplified by the structure of photosystem I from a high-light tolerant cyanobacteria, demonstrating the relationship between the structure and function in photosystem I.

Synechocystis switches its redox pools under reducing photomixotrophic conditions from utilizing NAD(H)- to ferredoxin-dependent enzymes and thereby balances its metabolism in a trade-off between energy conservation and chemical driving forces.

Phototrophic growth laws are elucidated by combining computational modeling and experiments for quantitative evaluation of cellular physiology, morphology and proteome allocation across a wide range of light conditions.

cyAbrB2, the global transcriptional factor conserved in cyanobacteria, is the nucleoid-associated protein, which is the first report in cyanobacteria.

The cells of a cyanobacterium act as spherical micro-lenses, allowing the cell to see a light source and move towards it.

Primordial cyanobacterial PSI structure.

The cyanobacterium Synechocystis secretes a specific sulphated polysaccharide to form floating cell aggregates.